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Protein Structure
A protein may consist of one or more poly peptide chains. The
different levels of structural organization shown by proteins are
primary, secondary tertiary and quaternary.
Primary structure.
The primary structure refers to the number, nature and sequence of
amino acids in the polypeptide chain or chains that constitute the
protein. Every polypeptide carries a free amino group at one end and a
free carboxyl group at the opposite end. The end at amino group is
termed amino-terminal end while the carboxyl end is termed carboxy
terminal end.
Secondary Structure.
It refers to the folding and twisting of the polypeptide chain brought
about primarily by hydrogen bonds between amide (NH) and carbonyl
(C=0) groups. Two basic types of secondary structures, namely α helix
and β pleated sheet.
α-helix.
In α-helix, polypeptide chains assume a spiral or spring like
conformation. Each turn of the α helix is consists of 3.6 aminoacid
residues. The amino acid is 1.5 A 0 . Α helix are linked by hydrogen
bonds.
B-Pleated sheet.
Proteins appears to be pleated because of the special arrangement of
the polypeptide chain. Poly-peptide chains are almost fully extended.
The distance between adjacent aminoacid is 3.5 A 0 . β conformation is
stabilized by hydrogen bond.
Tertiary Structure
The Poly peptide chain often undergoes further coiling and folding to
produce the tertiary structure. It is the three dimensional structure.
The tertiary structure is stabilized by several types of bonds, namely
hydrogen bonds, ionic bonds, hydrophobic interactions, van der waals
forces and disulphide linkages.
Eg: - Myoglobin.
Quaternary Structure
Quaternary structure is displayed by proteins containing more than one
polypeptide chains. Weak bonds such as hydrogen bonds, ionic bonds,
hydrophobic interactions and van der waals forces are responsible for
quaternary structure.
Eg:- Haemoglobin
Quaternary structure may be categorized into homogeneous and
heterogenous types.
In homogeneous class all the sub units are identical .
Eg;- Phoshorylase
In heterogeneous class the subunits are not alike.
Eg:- Insulin and haemoglobin.
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